ID   PLYA_ASPNG              Reviewed;         323 AA.
AC   Q9C2Z0;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Pectate lyase A;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=plyA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], GLYCOSYLATION, FUNCTION, COFACTOR, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=11112543; DOI=10.1021/bi000693w;
RA   Benen J.A., Kester H.C., Parenicova L., Visser J.;
RT   "Characterization of Aspergillus niger pectate lyase A.";
RL   Biochemistry 39:15563-15569(2000).
CC   -!- FUNCTION: Pectinolytic enzyme consist of four classes of enzymes:
CC       pectin lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the
CC       most important in depolymerization of pectin, since it cleaves internal
CC       glycosidic bonds of highly methylated pectins. Favors pectate, the
CC       anion, over pectin, the methyl ester. {ECO:0000269|PubMed:11112543}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC         oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC         their non-reducing ends.; EC=4.2.2.2;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:11112543};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11112543};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ276331; CAC33162.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9C2Z0; -.
DR   SMR; Q9C2Z0; -.
DR   STRING; 5061.CADANGAP00008167; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   CLAE; PLY1A_ASPNG; -.
DR   VEuPathDB; FungiDB:An10g00870; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1090563; -.
DR   VEuPathDB; FungiDB:ATCC64974_63830; -.
DR   VEuPathDB; FungiDB:M747DRAFT_374887; -.
DR   eggNOG; ENOG502S66G; Eukaryota.
DR   BioCyc; MetaCyc:MON-20558; -.
DR   BRENDA; 4.2.2.2; 518.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030570; F:pectate lyase activity; IDA:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Glycoprotein; Lyase; Metal-binding; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..31
FT   CHAIN           32..323
FT                   /note="Pectate lyase A"
FT                   /id="PRO_5000066020"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000255"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   323 AA;  34369 MW;  E7F438D307B816F2 CRC64;
     MTNFKWIVAA AGLLFGQVLA APTATSTHAK RATVSDAAFG YASLNGGTTG GAGGTTTTVS
     SYAAFTSAVS GDDAKVVYVD GTIKQTADQV KIGSNTSIIG KDANAILEGF GVLVKEKENV
     IIRNLGVSKV LADNGDAIGV QYSNNVWIDH CDVSSDRDHD KDYYDGLIDI THGSDYVTVS
     NTFIHDHWKA SLVGHSDSNE DEDSGHLTVT YANNYWYNVN SRAPSFRFGT GHVYNSYYLD
     VSDGINTRDG AQLLVESNQF VDSKKALYST DDGYAVSNDN DFGDSENTAE EGTLTSMPYD
     YTLLGSANVK AAVVGTAGQT LTF